Cytochrome P450 and arachidonic acid bioactivation: Molecular and functional properties of the arachidonate monooxygenase

Jorge H. Capdevila, J R Falck, Raymond C. Harris

Research output: Contribution to journalReview article

416 Scopus citations

Abstract

The demonstration of in vivo arachidonic acid epoxidation and ω- hydroxylation established the cytochrome P450 epoxygenase and ω/ω-1 hydroxylase as formal metabolic pathways and as members of the arachidonate metabolic cascade. The characterization of the potent biological activities associated with several of the cytochrome P450-derived eicosanoids suggested new and important functional roles for these enzymes in cellular, organ, and body physiology, including the control of vascular reactivity and systemic blood pressures. Past and current advances in cytochrome P450 biochemistry and molecular biology facilitate the characterization of cytochrome P450 isoforms responsible for tissue/organ specific arachidonic acid epoxidation and ω/ω-1 hydroxylation, and thus, the analysis of cDNA and/or gene specific functional phenotypes. The combined application of physiological, biochemical, molecular, and genetic approaches is beginning to provide new insights into the physiological and/or pathophysiological significance of these enzymes, their endogenous substrates, and products.

Original languageEnglish (US)
Pages (from-to)163-181
Number of pages19
JournalJournal of lipid research
Volume41
Issue number2
StatePublished - Feb 1 2000

    Fingerprint

Keywords

  • Arachidonic acid
  • Arachidonic acid epoxygenase
  • Arachidonic acid monooxygenase
  • Cytochrome P450
  • EDHF
  • EET
  • Eicosanoids
  • Fatty acid hydroxylase
  • HETE
  • Hyperpolarizing factor
  • Hypertension
  • Salt sensitivity

ASJC Scopus subject areas

  • Biochemistry
  • Endocrinology
  • Cell Biology

Cite this